9OZZ
Flavobacterium johnsoniae 70S initiation complex with rpsU mRNA containing Shine-Dalgarno sequence. State 2.
This is a non-PDB format compatible entry.
Summary for 9OZZ
| Entry DOI | 10.2210/pdb9ozz/pdb |
| EMDB information | 71061 |
| Descriptor | 23S rRNA, 50S ribosomal protein L4, 50S ribosomal protein L5, ... (55 entities in total) |
| Functional Keywords | ribosome, 70s, initiation complex, translation. |
| Biological source | Flavobacterium johnsoniae More |
| Total number of polymer chains | 55 |
| Total formula weight | 2190270.67 |
| Authors | |
| Primary citation | Arpin, D.,Roy, B.,Naeem, F.M.,Fredrick, K.,Ortega, J. Structure of a specialized 70S initiation complex. Nucleic Acids Res., 54:-, 2026 Cited by PubMed Abstract: Bacteria of class Bacteroidia lack Shine-Dalgarno (SD) sequences and instead rely on other messenger RNA (mRNA) features, including upstream adenines, for start codon selection. Bacteroidia ribosomes contain the anti-SD (ASD) sequence of 16S ribosomal RNA (rRNA) but are "blind" to SD sequences. This occurs due to the sequestration of the ASD through interactions with bS21, bS18, and bS6 on the 30S platform domain. In many Bacteroidia, including Flavobacterium johnsoniae, there is one gene with an extended SD-rpsU, which encodes bS21. Ribosomes lacking bS21 exhibit high-level translation of rpsU, establishing an autoregulatory circuit in the cell. In this work, we investigate the structural basis of initiation on rpsU mRNA. We find using cryo-electron microscopy that initiation entails the formation of a 13-base pair SD-ASD helix that sterically occludes bS21. Mutations of bS21, bS18, or bS6 that compromise the platform pocket liberate the 3' tail of 16S rRNA, enable SD-ASD pairing, and enhance initiation. As initiation on rpsU mRNA depends on SD-ASD pairing, we infer that dissociation of bS21 from replete ribosomes limits their initiation rate. This work shows how a compositional change of the ribosome can govern translation of a specific gene. PubMed: 41854077DOI: 10.1093/nar/gkag094 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.5 Å) |
Structure validation
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